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Modelling the p53/p66Shc Aging Pathway in the Shortest Living
Vertebrate Nothobranchius Furzeri
Chiara Priami 1, 3 ;Giulia De Michele 1 ;Franco Cotelli 3 ;Alessandro Cellerino 4 ;Marco Giorgio 1 ;Pier Giuseppe Pelicci 1, 2 ;Enrica
Migliaccio 1 ;
1 European Institute of Oncology, Via Ripamonti 435, 20141 Milan, Italy. ; 2 Dipartimento di Medicina, Chirurgia e Odontoiatria,
University of Milan, Italy ; 3 Dipartimento di Bioscienze, University of Milan, Italy. ; 4 Scuola Normale Superiore, Pisa, Italy ;
Figure 4. Modular organization of p66Shc orthologs of different vertebrate species . CH2, light green: Collagen Homology 2 domain; PTB, red: Phosphotyrosine Binding
Domain; CH1, light blue: Collagen Homology 1 domain; SH2, yellow: Src homology 2 domain. Note that a CH2 region is present in all the vertebrate species, whereas it is
absent or not recognizable in invertebrates. Post-translational modified amino acid residues are indicated: serines with a pink spot, threonines with a blue spot and tyrosines
with a light green spot. For Homo sapiens, it is also indicated the position in the sequence and the type of post-translational modification P=phosphorylation. Amino acids of
the human sequence are also numbered from 1 to 7: in other sequences than human, conserved amino acid residues are indicated only with the corresponding number and
Aging
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Doi:10.14336/AD.2014.0228
not with
position in their sequence.
Amino acids are considered conserved even if they are substituted with a functionally similar one: T386 is not found in X. tropicalis,
but this amino acid is here substituted with a serine, thus the number 6 is the same, but the color of the spot changes from blue to pink. The Cytochrome c Binding CB
domain is indicated with a yellow pentagon with the amino acids of the core: EEW in H. sapiens and M. musculus, DEW in X. tropicalis, N. furzeri and D. rerio. Starting site of
the p52Shc isoform is also indicated with an arrow.